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Article ; Online: Detergent micelle conjugates containing amino acid monomers allow purification of human IgG near neutral pH.

Dhandapani, Gunasekaran / Wachtel, Ellen / Patchornik, Guy

Journal of chromatography. B, Analytical technologies in the biomedical and life sciences

2022 Volume 1206, Page(s) 123358

Abstract: Industrial scale production of therapeutic monoclonal antibodies (mAbs) is commonly achieved with Protein A chromatography, a process that requires exposure of the antibody to strongly acidic conditions during the eluting step. Exposure to acid ... ...

Abstract	Industrial scale production of therapeutic monoclonal antibodies (mAbs) is commonly achieved with Protein A chromatography, a process that requires exposure of the antibody to strongly acidic conditions during the eluting step. Exposure to acid inactivates virus contaminants but may, in parallel, lead to antibody aggregation that must be eliminated or kept at acceptably low levels. This report seeks to provide a practical method for overcoming a long-standing problem. We show how Brij-O20 detergent micelles, conjugated by the amphiphilic [(bathophenanthroline)
MeSH term(s)	Amino Acids ; Detergents ; Humans ; Hydrogen-Ion Concentration ; Immunoglobulin G ; Micelles ; Tyrosine
Chemical Substances	Amino Acids ; Detergents ; Immunoglobulin G ; Micelles ; Tyrosine (42HK56048U)
Language	English
Publishing date	2022-06-28
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	1180823-8
ISSN	1873-376X ; 0378-4347 ; 1570-0232 ; 1387-2273
ISSN (online)	1873-376X
ISSN	0378-4347 ; 1570-0232 ; 1387-2273
DOI	10.1016/j.jchromb.2022.123358
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Article: Detergent micelle conjugates containing amino acid monomers allow purification of human IgG near neutral pH

Dhandapani, Gunasekaran / Wachtel, Ellen / Patchornik, Guy

Journal of chromatography. 2022 Aug. 15, v. 1206

2022

Abstract	Industrial scale production of therapeutic monoclonal antibodies (mAbs) is commonly achieved with Protein A chromatography, a process that requires exposure of the antibody to strongly acidic conditions during the eluting step. Exposure to acid inactivates virus contaminants but may, in parallel, lead to antibody aggregation that must be eliminated or kept at acceptably low levels. This report seeks to provide a practical method for overcoming a long-standing problem. We show how Brij-O20 detergent micelles, conjugated by the amphiphilic [(bathophenanthroline)₃:Fe²⁺] complex in the presence of amino acid monomers: phenylalanine (Phe), tyrosine (Tyr), tryptophan (Trp), isoleucine (Ile) or valine (Val), efficiently capture polyclonal human IgG (hIgG) at neutral pH and allow its recovery by extraction either at pH 4 (85–97% yield) or at pH 6.3 (72–84% yield). Of the five amino acid monomers surveyed, Phe or Tyr produced the highest overall process yield at both pH 4 and 6.3. The monomeric state of the purified hIgG's was confirmed by dynamic light scattering (DLS). Potential advantages of the purification method are discussed.
Keywords	chromatography ; detergents ; humans ; isoleucine ; micelles ; pH ; phenylalanine ; purification methods ; therapeutics ; tryptophan ; tyrosine ; valine ; viruses
Language	English
Dates of publication	2022-0815
Publishing place	Elsevier B.V.
Document type	Article
ISSN	1570-0232
DOI	10.1016/j.jchromb.2022.123358
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Article ; Online: Conjugated detergent micelles as a platform for IgM purification.

Dhandapani, Gunasekaran / Wachtel, Ellen / Das, Ishita / Sheves, Mordechai / Patchornik, Guy

Biotechnology and bioengineering

2022 Volume 119, Issue 7, Page(s) 1997–2003

Abstract: Immunoglobulin M (IgM) antibodies hold promise as anticancer drugs and as agents for promoting immune homeostasis. This promise has not been realized due to low expression levels in mammalian cells producing IgM class antibodies, and the failure of ... ...

Abstract	Immunoglobulin M (IgM) antibodies hold promise as anticancer drugs and as agents for promoting immune homeostasis. This promise has not been realized due to low expression levels in mammalian cells producing IgM class antibodies, and the failure of protein A chromatography for IgM purification. Here, we describe a nonchromatographic platform for quantitatively capturing IgMs at neutral pH, which is then recovered with 86%-94% yield and >95% purity at pH 3. The platform contains micelles conjugated with the [(bathophenanthroline)
MeSH term(s)	Animals ; Antibodies, Monoclonal/metabolism ; Cattle ; Detergents ; Humans ; Immunoglobulin M/metabolism ; Mammals/metabolism ; Micelles ; Staphylococcal Protein A
Chemical Substances	Antibodies, Monoclonal ; Detergents ; Immunoglobulin M ; Micelles ; Staphylococcal Protein A
Language	English
Publishing date	2022-04-04
Publishing country	United States
Document type	Journal Article
ZDB-ID	280318-5
ISSN	1097-0290 ; 0006-3592
ISSN (online)	1097-0290
ISSN	0006-3592
DOI	10.1002/bit.28089
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Article ; Online: Nonionic detergent micelle aggregates: An economical alternative to protein A chromatography.

Dhandapani, Gunasekaran / Wachtel, Ellen / Sheves, Mordechai / Patchornik, Guy

New biotechnology

2020 Volume 61, Page(s) 90–98

Abstract: We have recently described a non-chromatographic, ligand-free approach for antibody (Ab) purification based on specially designed [Tween-20:bathophenanthroline: ... ...

Abstract	We have recently described a non-chromatographic, ligand-free approach for antibody (Ab) purification based on specially designed [Tween-20:bathophenanthroline:Fe
Language	English
Publishing date	2020-12-03
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2400836-9
ISSN	1876-4347 ; 1871-6784
ISSN (online)	1876-4347
ISSN	1871-6784
DOI	10.1016/j.nbt.2020.11.013
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Article ; Online: Purification of antibody fragments via interaction with detergent micellar aggregates.

Dhandapani, Gunasekaran / Wachtel, Ellen / Das, Ishita / Sheves, Mordechai / Patchornik, Guy

Scientific reports

2021 Volume 11, Issue 1, Page(s) 11697

Abstract: The research described in this report seeks to present proof-of-concept for a novel and robust platform for purification of antibody fragments and to define and optimize the controlling parameters. Purification of antigen-binding F(ab') ...

Abstract	The research described in this report seeks to present proof-of-concept for a novel and robust platform for purification of antibody fragments and to define and optimize the controlling parameters. Purification of antigen-binding F(ab')
MeSH term(s)	Antibodies, Monoclonal/chemistry ; Chromatography, Affinity ; Escherichia coli/metabolism ; Immunoglobulin Fab Fragments/chemistry ; Immunoglobulin Fc Fragments/chemistry ; Immunoglobulin Fragments/metabolism ; Immunoglobulin G/chemistry ; Micelles ; Staphylococcal Protein A/chemistry
Chemical Substances	Antibodies, Monoclonal ; Immunoglobulin Fab Fragments ; Immunoglobulin Fc Fragments ; Immunoglobulin Fragments ; Immunoglobulin G ; Micelles ; Staphylococcal Protein A
Language	English
Publishing date	2021-06-03
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-021-90966-1
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Article ; Online: Leptospiral cell wall hydrolase (LIC_10271) binding peptidoglycan, lipopolysaccharide, and laminin and the protein show LysM and M23 domains are co-existing in pathogenic species.

Sarma, Abhijit / Dhandapani, Gunasekaran / Phukan, Homen / Bhunia, Prasun Kumar / De, Arun Kumar / Bhattacharya, Debasis / Jebasingh, T / Madanan, Madathiparambil G

Research in microbiology

2023 Volume 174, Issue 8, Page(s) 104107

Abstract: Leptospirosis, a global reemerging zoonosis caused by the spirochete Leptospira, has severe human and veterinary implications. Cell wall hydrolase (LIC_10271) with LytM (peptidase M23) and LysM domains are found to be associated with various pathogenic ... ...

Abstract	Leptospirosis, a global reemerging zoonosis caused by the spirochete Leptospira, has severe human and veterinary implications. Cell wall hydrolase (LIC_10271) with LytM (peptidase M23) and LysM domains are found to be associated with various pathogenic bacteria. These domains regulate effects on extracellular matrix and biofilm components, which promote cell wall remodeling and pathogen dissemination in the host. In this study, we present the cloning, expression, purification, and characterization of LIC_10271. To determine the localization of LIC_10271 within the inner membrane of Leptospira, Triton X-114 subcellular fractionation and immunoblot studies were performed. Furthermore, r-LIC_10271 binds with peptidoglycan, lipopolysaccharide, and laminin in a dose-dependent manner. Analysis of the signal peptide, M23, and LysM domains revealed conservation primarily within the P1 group of Leptospira, which encompasses the most pathogenic species. Moreover, the presence of native-LIC_10271 in the inner membrane and the distribution of M23 and LysM domains across pathogenic strains indicates their potential involvement in the interaction between the host and Leptospira.
MeSH term(s)	Humans ; Laminin/metabolism ; Lipopolysaccharides/metabolism ; Peptidoglycan/metabolism ; Leptospira interrogans/genetics ; Leptospira interrogans/metabolism ; Hydrolases/metabolism ; Leptospira/genetics ; Cell Wall/metabolism ; Protein Binding
Chemical Substances	Laminin ; Lipopolysaccharides ; Peptidoglycan ; Hydrolases (EC 3.-)
Language	English
Publishing date	2023-07-28
Publishing country	France
Document type	Journal Article
ZDB-ID	1004220-9
ISSN	1769-7123 ; 0923-2508
ISSN (online)	1769-7123
ISSN	0923-2508
DOI	10.1016/j.resmic.2023.104107
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Article ; Online: Role of amphiphilic [metal:chelator] complexes in a non-chromatographic antibody purification platform.

Dhandapani, Gunasekaran / Nair, Divya K / Kale, Raju R / Wachtel, Ellen / Namboothiri, Irishi N N / Patchornik, Guy

Journal of chromatography. B, Analytical technologies in the biomedical and life sciences

2019 Volume 1133, Page(s) 121830

Abstract: We have recently introduced a non-chromatographic alternative for antibody (Ab) purification, one which does not require the use of Protein A. With this approach, polyclonal human or mouse immunoglobulins (IgG's) are captured almost quantitatively by ... ...

Abstract	We have recently introduced a non-chromatographic alternative for antibody (Ab) purification, one which does not require the use of Protein A. With this approach, polyclonal human or mouse immunoglobulins (IgG's) are captured almost quantitatively by Tween-20 micelles conjugated with a [chelator:divalent metal cation] complex. Target IgG structure remains native even following extraction from the surfactant aggregate. In the present work, we explore the effect of varying both components of the [metal:chelator] pair on the yield of purified Ab. Capture efficiency is observed to correlate with the formation of sufficiently large detergent aggregates, as determined by dynamic light scattering (DLS) and polyacrylamide gel electrophoresis (PAGE). This, in turn, depends on the rigidity and aromaticity of the chelator. Detergent aggregates are stable over a wide range of pH values (pH = 3-9). Under acidic conditions (3-3.8) they lead to good IgG recovery yields (70-78%) with purity similar to that obtained with Protein A chromatography while maintaining the monomeric state of the IgG's. Finally, the influence of the environment and the presence of various water-soluble chelators (e.g. EDTA, histidine, imidazole) on process efficiency, is described.
MeSH term(s)	Animals ; Chelating Agents/chemistry ; Chromatography, Affinity ; Electrophoresis, Polyacrylamide Gel ; Humans ; Hydrogen-Ion Concentration ; Immunoglobulin G/isolation & purification ; Metals/chemistry ; Mice ; Micelles ; Polysorbates ; Staphylococcal Protein A/chemistry ; Staphylococcal Protein A/metabolism
Chemical Substances	Chelating Agents ; Immunoglobulin G ; Metals ; Micelles ; Polysorbates ; Staphylococcal Protein A
Language	English
Publishing date	2019-10-21
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	1180823-8
ISSN	1873-376X ; 0378-4347 ; 1570-0232 ; 1387-2273
ISSN (online)	1873-376X
ISSN	0378-4347 ; 1570-0232 ; 1387-2273
DOI	10.1016/j.jchromb.2019.121830
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Tuberculous otitis media and staphylococcus aureus coinfection in a five-year-old boy with miliary tuberculosis

Gopalakrishnan Manigandan / Chandrasekaran Venkatesh / Dhandapani Gunasekaran / Palanisamy Soundararajan

Journal of Global Infectious Diseases, Vol 5, Iss 1, Pp 26-

2013 Volume 28

Abstract: A five-year-old boy with acute on chronic ear discharge and fever was diagnosed to have tubercular otitis media (TOM) with Staphylococcus aureus co-infection. His chest X-ray was suggestive of miliary tuberculosis. The clinical presentation of the child ... ...

Abstract	A five-year-old boy with acute on chronic ear discharge and fever was diagnosed to have tubercular otitis media (TOM) with Staphylococcus aureus co-infection. His chest X-ray was suggestive of miliary tuberculosis. The clinical presentation of the child with a brief review of the literature pertaining to the case is being discussed in this report.
Keywords	Child ; Miliary tuberculosis ; Otitis media ; Staphylococcus aureus ; Tuberculous ; Infectious and parasitic diseases ; RC109-216 ; Internal medicine ; RC31-1245 ; Medicine ; R
Language	English
Publishing date	2013-01-01T00:00:00Z
Publisher	Wolters Kluwer Medknow Publications
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Extracellular Proteome Analysis Shows the Abundance of Histidine Kinase Sensor Protein, DNA Helicase, Putative Lipoprotein Containing Peptidase M75 Domain and Peptidase C39 Domain Protein in Leptospira interrogans Grown in EMJH Medium

Abhijit Sarma / Dhandapani Gunasekaran / Devasahayam Arokia Balaya Rex / Thoduvayil Sikha / Homen Phukan / Kumar Mangalaparthi Kiran / Sneha M. Pinto / Thottethodi Subrahmanya Keshava Prasad / Madathiparambil G. Madanan

Pathogens, Vol 10, Iss 852, p

2021 Volume 852

Abstract: Leptospirosis is a re-emerging form of zoonosis that is caused by the spirochete pathogen Leptospira . Extracellular proteins play critical roles in the pathogenicity and survival of this pathogen in the host and environment. Extraction and analysis of ... ...

Abstract	Leptospirosis is a re-emerging form of zoonosis that is caused by the spirochete pathogen Leptospira . Extracellular proteins play critical roles in the pathogenicity and survival of this pathogen in the host and environment. Extraction and analysis of extracellular proteins is a difficult task due to the abundance of enrichments like serum and bovine serum albumin in the culture medium, as is distinguishing them from the cellular proteins that may reach the analyte during extraction. In this study, extracellular proteins were separated as secretory proteins from the culture supernatant and surface proteins were separated during the washing of the cell pellet. The proteins identified were sorted based on the proportion of the cellular fractions and the extracellular fractions. The results showed the identification of 56 extracellular proteins, out of which 19 were exclusively extracellular. For those proteins, the difference in quantity with respect to their presence within the cell was found to be up to 1770-fold. Further, bioinformatics analysis elucidated characteristics and functions of the identified proteins. Orthologs of extracellular proteins in various Leptospira species were found to be closely related among different pathogenic forms. In addition to the identification of extracellular proteins, this study put forward a method for the extraction and identification of extracellular proteins.
Keywords	Leptospira ; protein ; extracellular ; surface ; secretory ; pathogenic ; Medicine ; R
Subject code	500 ; 580
Language	English
Publishing date	2021-07-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article: Role of Amphiphilic [Metal:Chelator] Complexes in a Non-Chromatographic Antibody Purification Platform

Dhandapani, Gunasekaran / Nair, Divya K / Kale, Raju R / Wachtel, Ellen / N. N. Namboothiri, Irishi / Patchornik, Guy

Journal of chromatography. 2019 Oct. 11,

2019

Abstract	We have recently introduced a non-chromatographic alternative for antibody (Ab) purification, one which does not require the use of Protein A. With this approach, polyclonal human or mouse immunoglobulins (IgG’s) are captured almost quantitatively by Tween-20 micelles conjugated with a [chelator:divalent metal cation] complex. Target IgG structure remains native even following extraction from the surfactant aggregate. In the present work, we explore the effect of varying both components of the [metal:chelator] pair on the yield of purified Ab. Capture efficiency is observed to correlate with the formation of sufficiently large detergent aggregates, as determined by dynamic light scattering (DLS) and polyacrylamide gel electrophoresis (PAGE). This, in turn, depends on the rigidity and aromaticity of the chelator. Detergent aggregates are stable over a wide range of pH values (pH = 3-9). Under acidic conditions (3-3.8) they lead to good IgG recovery yields (70-78%) with purity similar to that obtained with Protein A chromatography while maintaining the monomeric state of the IgG's. Finally, the influence of the environment and the presence of various water-soluble chelators (e.g. EDTA, histidine, imidazole) on process efficiency, is described.
Keywords	EDTA (chelating agent) ; antibodies ; chelating agents ; chromatography ; detergents ; histidine ; humans ; imidazole ; immunoglobulin G ; light scattering ; metal ions ; mice ; micelles ; pH ; polyacrylamide gel electrophoresis ; polysorbates ; surfactants ; water solubility
Language	English
Dates of publication	2019-1011
Publishing place	Elsevier B.V.
Document type	Article
Note	Pre-press version
ISSN	1570-0232
DOI	10.1016/j.jchromb.2019.121830
Database	NAL-Catalogue (AGRICOLA)

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